Ubiquitin thioesterase OTUB1 Recombinant Protein | OTUB1 recombinant protein

Recombinant Human Ubiquitin thioesterase OTUB1

Cat. Num. AAA717257

• Gene Names: OTUB1; OTB1; OTU1; HSPC263
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Ubiquitin thioesterase OTUB1; Recombinant Human Ubiquitin thioesterase OTUB1; Deubiquitinating enzyme OTUB1OTU domain-containing ubiquitin aldehyde-binding protein 1; Otubain-1; hOTU1; Ubiquitin-specific-processing protease OTUB1; OTUB1 recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 2-201aa; Partial
• Sequence: AAEEPQQQKQEPLGSDSEGVNCLAYDEAIMAQQDRIQQEIAVQNPLVSERLELSVLYKEYAEDDNIYQQKIKDLHKKYSYIRKTRPDGNCFYRAFGFSHLEALLDDSKELQRFKAVSAKSKEDLVSQGFTEFTIEDFHNTFMDLIEQVEKQTSVADLLASFNDQSTSDYLVVYLRLLTSGYLQRESKFFEHFIEGGRTVK
• Sequence Length: 271

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for OTUB1 recombinant protein

Hydrolase that can specifically rove 'Lys-48'-linked conjugated ubiquitin from proteins and plays an important regulatory role at the level of protein turnover by preventing degradation. Regulator of T-cell anergy, a phenomenon that occurs when T-cells are rendered unresponsive to antigen rechallenge and no longer respond to their cognate antigen. Acts via its interaction with RNF128/GRAIL, a crucial inductor of CD4 T-cell anergy. Isoform 1 destabilizes RNF128, leading to prevent anergy. In contrast, isoform 2 stabilizes RNF128 and promotes anergy. Surprisingly, it regulates RNF128-mediated ubiquitination, but does not deubiquitinate polyubiquitinated RNF128. Deubiquitinates estrogen receptor alpha (ESR1). Mediates deubiquitination of 'Lys-48'-linked polyubiquitin chains, but not 'Lys-63'-linked polyubiquitin chains. Not able to cleave di-ubiquitin. Also capable of roving NEDD8 from NEDD8 conjugates, but with a much lower preference compared to 'Lys-48'-linked ubiquitin. Plays a key non-catalytic role in DNA repair regulation by inhibiting activity of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites. Inhibits RNF168 independently of ubiquitin thioesterase activity by binding and inhibiting UBE2N/UBC13, the E2 partner of RNF168, thereby limiting spreading of 'Lys-63'-linked histone H2A and H2AX marks. Inhibition occurs by binding to free ubiquitin: free ubiquitin acts as an allosteric regulator that increases affinity for UBE2N/UBC13 and disrupts interaction with UBE2V1. The OTUB1-UBE2N/UBC13-free ubiquitin complex adopts a configuration that mimics a cleaved 'Lys48'-linked di-ubiquitin chain.

Product Categories/Family for OTUB1 recombinant protein

Immunology

References

Otubains a new family of cysteine proteases in the ubiquitin pathway.Balakirev M.Y., Tcherniuk S.O., Jaquinod M., Chroboczek J.EMBO Rep. 4:517-522(2003) Two isoforms of otubain 1 regulate T cell anergy via GRAIL.Soares L., Seroogy C., Skrenta H., Anandasabapathy N., Lovelace P., Chung C.D., Engleman E., Fathman C.G.Nat. Immunol. 5:45-54(2004) Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells.Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.Genome Res. 10:1546-1560(2000) Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) Human chromosome 11 DNA sequence and analysis including novel gene identification.Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.Nature 440:497-500(2006) Chemistry-based functional proteomics reveals novel members of the deubiquitinating enzyme family.Borodovsky A., Ovaa H., Kolli N., Gan-Erdene T., Wilkinson K.D., Ploegh H.L., Kessler B.M.Chem. Biol. 9:1149-1159(2002) A quantitative atlas of mitotic phosphorylation.Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.Anal. Chem. 81:4493-4501(2009) OTU Domain-containing ubiquitin aldehyde-binding protein 1 (OTUB1) deubiquitinates estrogen receptor (ER) alpha and affects ERalpha transcriptional activity.Stanisic V., Malovannaya A., Qin J., Lonard D.M., O'Malley B.W.J. Biol. Chem. 284:16135-16145(2009) Evidence for bidentate substrate binding as the basis for the K48 linkage specificity of otubain 1.Wang T., Yin L., Cooper E.M., Lai M.-Y., Dickey S., Pickart C.M., Fushman D., Wilkinson K.D., Cohen R.E., Wolberger C.J. Mol. Biol. 386:1011-1023(2009) Non-canonical inhibition of DNA damage-dependent ubiquitination by OTUB1.Nakada S., Tai I., Panier S., Al-Hakim A., Iemura S., Juang Y.C., O'Donnell L., Kumakubo A., Munro M., Sicheri F., Gingras A.C., Natsume T., Suda T., Durocher D.Nature 466:941-946(2010) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) OTU deubiquitinases reveal mechanisms of linkage specificity and enable ubiquitin chain restriction analysis.Mevissen T.E., Hospenthal M.K., Geurink P.P., Elliott P.R., Akutsu M., Arnaudo N., Ekkebus R., Kulathu Y., Wauer T., El Oualid F., Freund S.M., Ovaa H., Komander D.Cell 154:169-184(2013) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) Structural basis and specificity of human otubain 1-mediated deubiquitination.Edelmann M.J., Iphoefer A., Akutsu M., Altun M., di Gleria K., Kramer H.B., Fiebiger E., Dhe-Paganon S., Kessler B.M.Biochem. J. 418:379-390(2009) OTUB1 co-opts Lys48-linked ubiquitin recognition to suppress E2 enzyme function.Juang Y.C., Landry M.C., Sanches M., Vittal V., Leung C.C., Ceccarelli D.F., Mateo A.R., Pruneda J.N., Mao D.Y., Szilard R.K., Orlicky S., Munro M., Brzovic P.S., Klevit R.E., Sicheri F., Durocher D.Mol. Cell 45:384-397(2012) The mechanism of OTUB1-mediated inhibition of ubiquitination.Wiener R., Zhang X., Wang T., Wolberger C.Nature 483:618-622(2012)

NCBI and Uniprot Product Information

• NCBI GI #: 109148508
• NCBI GeneID: 55611
• NCBI Accession #: NP_060140.2
• NCBI GenBank Nucleotide #: NM_017670.2
• UniProt Accession #: Q96FW1; Q32Q78; Q96II3; Q9NXQ4; Q9P0B8
• Molecular Weight: 50.1 kDa
• NCBI Official Full Name: ubiquitin thioesterase OTUB1
• NCBI Official Synonym Full Names: OTU deubiquitinase, ubiquitin aldehyde binding 1
• NCBI Official Symbol: OTUB1
• NCBI Official Synonym Symbols: OTB1; OTU1; HSPC263
• NCBI Protein Information: ubiquitin thioesterase OTUB1
• UniProt Protein Name: Ubiquitin thioesterase OTUB1
• Protein Family: Ubiquitin thioesterase
• UniProt Gene Name: OTUB1
• UniProt Synonym Gene Names: OTB1; OTU1; hOTU1
• UniProt Entry Name: OTUB1_HUMAN

NCBI Description

The product of this gene is a member of the OTU (ovarian tumor) superfamily of predicted cysteine proteases. The encoded protein is a highly specific ubiquitin iso-peptidase, and cleaves ubiquitin from branched poly-ubiquitin chains but not from ubiquitinated substrates. It interacts with another ubiquitin protease and an E3 ubiquitin ligase that inhibits cytokine gene transcription in the immune system. It is proposed to function in specific ubiquitin-dependent pathways, possibly by providing an editing function for polyubiquitin chain growth. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2008]

Uniprot Description

OTUB1: a protease that can remove conjugated ubiquitin from proteins in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Regulator of T-cell anergy, a phenomenon that occur when T-cell are rendered unresponsive to antigen rechallenge and no longer respond to their cognate antigen. Acts via its interaction with RNF128/GRAIL, a crucial inductor of CD4 T-cell anergy. Two alternatively spliced isoforms are known.

Protein type: Ubiquitin conjugating system; Protease; Ubiquitin-specific protease; EC 3.4.19.12

Chromosomal Location of Human Ortholog: 11q13.1

Cellular Component: cytoplasm; nucleus

Molecular Function: NEDD8-specific protease activity; protein binding; ubiquitin binding; ubiquitin protein ligase binding; ubiquitin-specific protease activity

Biological Process: adaptive immune response; DNA repair; response to DNA damage stimulus